Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1976 Sep 1;144(3):821–827. doi: 10.1084/jem.144.3.821

Endotoxin protein: a B-cell mitogen and polyclonal activator of C3H/HeJ lymphocytes

PMCID: PMC2190414  PMID: 784892

Abstract

A cell wall protein that is ordinarily complexed to the lipopolysaccharide endotoxin in gram-negative bacteria has been separated by the use of aqueous phenol. The protein is active as a B- cell mitogen and polyclonal activator of murine lymphocytes including the C3H/HeJ strain which is a nonresponder to lipoplysaccharide or lipid A.

Full Text

The Full Text of this article is available as a PDF (392.5 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andersson B., Blomgren H. Evidence for a small pool of immunocompetent cells in the mouse thymus. Its role in the humoral antibody response against sheep erythrocytes, bovine serum albumin, ovalbumin and the NIP determinant. Cell Immunol. 1970 Oct;1(4):362–371. doi: 10.1016/0008-8749(70)90014-6. [DOI] [PubMed] [Google Scholar]
  2. Braun V., Rehn K. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur J Biochem. 1969 Oct;10(3):426–438. doi: 10.1111/j.1432-1033.1969.tb00707.x. [DOI] [PubMed] [Google Scholar]
  3. Coutinho A., Gronowicz E., Sultzer B. M. Genetic control of B-cell responses. I. Selective unresponsiveness to lipopolysaccharide. Scand J Immunol. 1975;4(2):139–143. doi: 10.1111/j.1365-3083.1975.tb02610.x. [DOI] [PubMed] [Google Scholar]
  4. Freedman H. H., Fox A. E., Willis R. S., Schwartz B. S. Role of protein component of endotoxin in modification of host reactivity. Proc Soc Exp Biol Med. 1967 Aug-Sep;125(4):1316–1320. doi: 10.3181/00379727-125-32346. [DOI] [PubMed] [Google Scholar]
  5. Homma J. Y. The protein moiety of the endotoxin of Pseudomonas aeruginosa. Z Allg Mikrobiol. 1968;8(3):227–248. doi: 10.1002/jobm.3630080310. [DOI] [PubMed] [Google Scholar]
  6. KABAT E. A., SCHIFFMAN G. Immunochemical studies on blood groups. 28. Further studies on the oligosaccharide determinats of blood group B and BP1 specificity. J Immunol. 1962 Jun;88:782–787. [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. Melchers F., Braun V., Galanos C. The lipoprotein of the outer membrane of Escherichia coli: a B-lymphocyte mitogen. J Exp Med. 1975 Aug 1;142(2):473–482. doi: 10.1084/jem.142.2.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Nilsson B. S., Sultzer B. M., Bullock W. W. Purified protein derivative of tuberculin induces immunoglobulin production in normal mouse spleen cells. J Exp Med. 1973 Jan 1;137(1):127–139. doi: 10.1084/jem.137.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. OSBORN M. J. STUDIES ON THE GRAM-NEGATIVE CELL WALL. I. EVIDENCE FOR THE ROLE OF 2-KETO- 3-DEOXYOCTONATE IN THE LIPOPOLYSACCHARIDE OF SALMONELLA TYPHIMURIUM. Proc Natl Acad Sci U S A. 1963 Sep;50:499–506. doi: 10.1073/pnas.50.3.499. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. RONDLE C. J., MORGAN W. T. The determination of glucosamine and galactosamine. Biochem J. 1955 Dec;61(4):586–589. doi: 10.1042/bj0610586. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Rittenberg M. B., Pratt K. L. Antitrinitrophenyl (TNP) plaque assay. Primary response of Balb/c mice to soluble and particulate immunogen. Proc Soc Exp Biol Med. 1969 Nov;132(2):575–581. doi: 10.3181/00379727-132-34264. [DOI] [PubMed] [Google Scholar]
  13. Rosenstreich D. L., Glode L. M. Difference in B cell mitogen responsiveness between closely related strains of mice. J Immunol. 1975 Sep;115(3):777–780. [PubMed] [Google Scholar]
  14. Skidmore B. J., Chiller J. M., Morrison D. C., Weigle W. O. Immunologic properties of bacterial lipopolysaccharide (LPS): correlation between the mitogenic, adjuvant, and immunogenic activities. J Immunol. 1975 Feb;114(2 Pt 2):770–775. [PubMed] [Google Scholar]
  15. Sultzer B. M. Genetic analysis of lymphocyte activation by lipopolysaccharide Endotoxin. Infect Immun. 1976 Jun;13(6):1579–1584. doi: 10.1128/iai.13.6.1579-1584.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sultzer B. M. Genetic control of host responses to endotoxin. Infect Immun. 1972 Jan;5(1):107–113. doi: 10.1128/iai.5.1.107-113.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Sultzer B. M. Genetic factors in leucocyte responses to endotoxin: further studies in mice. J Immunol. 1969 Jul;103(1):32–38. [PubMed] [Google Scholar]
  18. Sultzer B. M., Nilsson B. S. PPD tuberculin--a B-cell mitogen. Nat New Biol. 1972 Dec 13;240(102):198–200. doi: 10.1038/newbio240198a0. [DOI] [PubMed] [Google Scholar]
  19. Taylor A., Knox K. W., Work E. Chemical and biological properties of an extracellular lipopolysaccharide from Escherichia coli grown under lysine-limiting conditions. Biochem J. 1966 Apr;99(1):53–61. doi: 10.1042/bj0990053. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wober W., Alaupović P. Studies on the protein moiety of endotoxin from gram-negative bacteria. Characterization of the protein moiety isolated by phenol treatment of endotoxin from Serratia marcescens 08 and Escherichia coli 0 141:K85(B). Eur J Biochem. 1971 Apr;19(3):340–356. doi: 10.1111/j.1432-1033.1971.tb01323.x. [DOI] [PubMed] [Google Scholar]
  21. Wu M. C., Heath E. C. Isolation and characterization of lipopolysaccharide protein from Escherichia coli. Proc Natl Acad Sci U S A. 1973 Sep;70(9):2572–2576. doi: 10.1073/pnas.70.9.2572. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES